메뉴 건너뛰기




Volumn 28, Issue 7-8, 2009, Pages 349-361

Study of cosolvent-induced α-chymotrypsin fibrillogenesis: Does protein surface hydrophobicity trigger early stages of aggregation reaction?

Author keywords

Aggregation; Fluorescence; Hydrophobicity; TFE; Chymotrypsin

Indexed keywords

AMYLOID; CHYMOTRYPSIN A;

EID: 72449140500     PISSN: 15723887     EISSN: 18758355     Source Type: Journal    
DOI: 10.1007/s10930-009-9200-5     Document Type: Article
Times cited : (21)

References (66)
  • 2
    • 11244340520 scopus 로고    scopus 로고
    • Thermally induced fibrillar aggregation of hen egg white lysozyme
    • DOI 10.1529/biophysj.104.048819
    • LN Arnaudov R de Vries 2005 Biophys J 88 515 526 10.1529/biophysj.104. 048819 (Pubitemid 40070697)
    • (2005) Biophysical Journal , vol.88 , Issue.1 , pp. 515-526
    • Arnaudov, L.N.1    De Vries, R.2
  • 4
    • 0030000385 scopus 로고    scopus 로고
    • The role of anti-inflammatory drugs in the prevention and treatment of Alzheimer's disease
    • DOI 10.1146/annurev.med.47.1.401
    • JCS Breitner 1996 Annu Rev Med 47 401 411 10.1146/annurev.med.47.1.401 (Pubitemid 26138900)
    • (1996) Annual Review of Medicine , vol.47 , pp. 401-411
    • Breitner, J.C.S.1
  • 8
    • 1642452936 scopus 로고    scopus 로고
    • Formation of amyloid fibrils from fully reduced hen egg white lysozyme
    • DOI 10.1110/ps.03183404
    • A Cao D Hu L Lai 2004 Protein Sci 13 319 324 10.1110/ps.03183404 (Pubitemid 38124952)
    • (2004) Protein Science , vol.13 , Issue.2 , pp. 319-324
    • Cao, A.1    Hu, D.2    Lai, L.3
  • 9
    • 0035085736 scopus 로고    scopus 로고
    • Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation
    • DOI 10.1110/ps.42401
    • F Chiti N Taddei M Stefani CM Dobson G Ramponi 2001 Protein Sci 10 879 886 10.1110/ps.42401 (Pubitemid 32240514)
    • (2001) Protein Science , vol.10 , Issue.4 , pp. 879-886
    • Chiti, F.1    Taddei, N.2    Stefani, M.3    Dobson, C.M.4    Ramponi, G.5
  • 10
    • 0031950560 scopus 로고    scopus 로고
    • Refolding of recombinant proteins
    • DOI 10.1016/S0958-1669(98)80109-2
    • EDB Clark 1998 Curr Opin Biotech 9 157 163 10.1016/S0958-1669(98)80109-2 (Pubitemid 28195001)
    • (1998) Current Opinion in Biotechnology , vol.9 , Issue.2 , pp. 157-163
    • Clark, E.D.B.1
  • 13
    • 0026459045 scopus 로고
    • 10.1021/ja00049a074
    • A Cooper 1992 J Am Chem Soc 114 9208 9209 10.1021/ja00049a074
    • (1992) J Am Chem Soc , vol.114 , pp. 9208-9209
    • Cooper, A.1
  • 15
    • 33646349196 scopus 로고    scopus 로고
    • Methods for enhancing the accuracy and reproducibility of Congo red and thioflavin T assays
    • DOI 10.1016/j.ab.2006.03.015, PII S0003269706001801
    • R Eisert L Felau LR Brown 2006 Anal Biochem 353 144 146 10.1016/j.ab.2006.03.015 (Pubitemid 43668937)
    • (2006) Analytical Biochemistry , vol.353 , Issue.1 , pp. 144-146
    • Eisert, R.1    Felau, L.2    Brown, L.R.3
  • 18
    • 0036135139 scopus 로고    scopus 로고
    • A possible role for π-stacking in the self-assembly of amyloid fibrils
    • DOI 10.1096/fj.01-0442hyp
    • E Gazit 2002 The FASEB J 16 77 83 10.1096/fj.01-0442hyp (Pubitemid 34027953)
    • (2002) FASEB Journal , vol.16 , Issue.1 , pp. 77-83
    • Gazit, E.1
  • 20
    • 0013889689 scopus 로고
    • 10.1016/0003-2697(66)90275-2
    • AFSA Habeeb 1966 Anal Biochem 14 328 336 10.1016/0003-2697(66)90275-2
    • (1966) Anal Biochem , vol.14 , pp. 328-336
    • Afsa, H.1
  • 21
    • 0036784667 scopus 로고    scopus 로고
    • A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea
    • DOI 10.1110/ps.0217702
    • D Hamada CM Dobson 2002 Protein Sci 11 2417 2426 10.1110/ps.0217702 (Pubitemid 35050667)
    • (2002) Protein Science , vol.11 , Issue.10 , pp. 2417-2426
    • Hamada, D.1    Dobson, C.M.2
  • 25
    • 0030778396 scopus 로고    scopus 로고
    • Hemin and related porphyrins inhibit β-amyloid aggregation
    • DOI 10.1016/S0014-5793(97)01290-8, PII S0014579397012908
    • D Howlett P Cutler S Heales P Camilleri 1997 FEBS Lett 417 249 251 10.1016/S0014-5793(97)01290-8 (Pubitemid 27491743)
    • (1997) FEBS Letters , vol.417 , Issue.2 , pp. 249-251
    • Howlett, D.1    Cutler, P.2    Heales, S.3    Camilleri, P.4
  • 30
    • 22544446791 scopus 로고    scopus 로고
    • Suppression effect of guanidine hydrochloride on α-cyclodextrin- assisted refolding of denatured α-amylase
    • DOI 10.1016/j.procbio.2005.01.018, PII S1359511305001376
    • R Khodarahmi R Yazdanparast 2005 Process Biochem 40 2973 2979 10.1016/j.procbio.2005.01.018 (Pubitemid 41009195)
    • (2005) Process Biochemistry , vol.40 , Issue.9 , pp. 2973-2979
    • Khodarahmi, R.1    Yazdanparast, R.2
  • 33
    • 72449174481 scopus 로고    scopus 로고
    • Medical Biology Research Center, Kermanshah University of Medical Sciences, (Unpublished data)
    • Khodarahmi R, Beyrami M, Naderi F, Medical Biology Research Center, Kermanshah University of Medical Sciences, (Unpublished data)
    • Khodarahmi, R.1    Beyrami, M.2    Naderi, F.3
  • 39
    • 0030711516 scopus 로고    scopus 로고
    • Crystal structure of phenylmethanesulfonyl fluoride-treated human chymase at 1.9 A
    • DOI 10.1021/bi971403n
    • ME McGrath T Mirzadegan BF Schmidt 1997 Biochemistry 36 14318 14324 10.1021/bi971403n (Pubitemid 27509923)
    • (1997) Biochemistry , vol.36 , Issue.47 , pp. 14318-14324
    • McGrath, M.E.1    Mirzadegan, T.2    Schmidt, B.F.3
  • 41
  • 43
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • DOI 10.1016/j.ymeth.2004.03.012, PII S104620230400060X
    • MR Nilsson 2004 Methods 34 151 160 10.1016/j.ymeth.2004.03.012 (Pubitemid 38993215)
    • (2004) Methods , vol.34 , Issue.1 , pp. 151-160
    • Nilsson, M.R.1
  • 44
    • 4143097041 scopus 로고    scopus 로고
    • Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin
    • DOI 10.1016/j.jmb.2004.06.089, PII S0022283604008460
    • I Pallares J Vendrell FX Aviles S Ventura 2004 J Mol Biol 342 321 331 10.1016/j.jmb.2004.06.089 (Pubitemid 39094523)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.1 , pp. 321-331
    • Pallars, I.1    Vendrell, J.2    Aviles, F.X.3    Ventura, S.4
  • 46
    • 1842790837 scopus 로고    scopus 로고
    • Aggregation of the acylphosphatase from Sulfolobus solfataricus: The folded and partially unfolded states can both be precursors for amyloid formation
    • DOI 10.1074/jbc.M312961200
    • G Plakoutsi N Taddei M Stefani F Chiti 2004 J Biol Chem 279 14111 14119 10.1074/jbc.M312961200 (Pubitemid 38468947)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.14 , pp. 14111-14119
    • Plakoutsi, G.1    Taddei, N.2    Stefani, M.3    Chiti, F.4
  • 47
    • 33745096194 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism
    • DOI 10.1111/j.1747-0285.2005.00318.x
    • Y Porat A Abramowitz E Gazit 2006 Chem Biol Drug Des 67 27 37 10.1111/j.1747-0285.2005.00318.x (Pubitemid 43881385)
    • (2006) Chemical Biology and Drug Design , vol.67 , Issue.1 , pp. 27-37
    • Porat, Y.1    Abramowitz, A.2    Gazit, E.3
  • 56
    • 33947708348 scopus 로고    scopus 로고
    • The molecular mechanisms of the anti-amyloid effects of phenols
    • DOI 10.1080/13506120601116674, PII 775701366
    • H Shoval D Lichtenberg E Gazit 2007 Amyloid 14 73 87 10.1080/ 13506120601116674 (Pubitemid 46491168)
    • (2007) Amyloid , vol.14 , Issue.1 , pp. 73-87
    • Shoval, H.1    Lichtenberg, D.2    Gazit, E.3
  • 58
    • 33749243722 scopus 로고    scopus 로고
    • Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway
    • DOI 10.1021/jm0606488
    • G Soldi G Plakoutsi N Taddei F Chiti 2006 J Med Chem 49 6057 6064 10.1021/jm0606488 (Pubitemid 44484949)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.20 , pp. 6057-6064
    • Soldi, G.1    Plakoutsi, G.2    Taddei, N.3    Chiti, F.4
  • 63
    • 0032572054 scopus 로고    scopus 로고
    • An indirect chaotropic mechanism for the stabilization of helix conformation of peptides in aqueous trifluoroethanol and hexafluoro-2- propanol
    • DOI 10.1021/ja973552z
    • R Walgers TC Lee A Cammers-Goodwin 1998 J Am Chem Soc 120 5073 5079 10.1021/ja973552z (Pubitemid 28281199)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.20 , pp. 5073-5079
    • Walgers, R.1    Lee, T.C.2    Cammers-Goodwin, A.3
  • 64
    • 0015859701 scopus 로고
    • 10.1016/0022-2836(73)90265-9
    • HT Wright 1973 J Mol Biol 79 1 11 10.1016/0022-2836(73)90265-9
    • (1973) J Mol Biol , vol.79 , pp. 1-11
    • Wright, H.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.